Biophysical Studies of Metalloenzymes

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The proposed biophysical studies comprises of two parts: electron-nuclear double resonance (endor) investigations of metalloenzymes; studies of long-range electron transfer within protein complexes. Dr. Hoffman is engaged in a program of multi- frequency cw and pulsed endor investigations of (i) the metal centers of hydrogenases, (ii) metalloenzymes from extreme thermophiles. Mixed-metal hemoglobin hybrids provide the optimal system for studying electron transfer within a rigid and crystallographically defined environment. Using this system Dr. Hoffman will examine the temperature response of electron transfer down to helium temperatures. He will also probe the interfacial conformational dynamics that control a cooperative binding transition displayed by non-covalent electron transfer complexes. %%% Endor spectroscopy is the technique of choice for answering many of the fundamental questions about the structure and function of metalloenzyme active sites. Long-range electron transfer is one of the most fundamental chemical and biological reactions, yet one of the most difficult to study.